(data stored in SCRATCH zone)

SWISSPROT: A8LF69_FRASN

ID   A8LF69_FRASN            Unreviewed;       471 AA.
AC   A8LF69;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571};
DE            Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01571};
GN   Name=proS {ECO:0000256|HAMAP-Rule:MF_01571};
GN   OrderedLocusNames=Franean1_0348 {ECO:0000313|EMBL:ABW09814.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09814.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC       two-step reaction: proline is first activated by ATP to form Pro-
CC       AMP and then transferred to the acceptor end of tRNA(Pro).
CC       {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-
CC         prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700,
CC         Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532,
CC         ChEBI:CHEBI:456215; EC=6.1.1.15; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01571};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC       domain, the anticodon-binding domain and the C-terminal extension.
CC       {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_01571}.
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DR   EMBL; CP000820; ABW09814.1; -; Genomic_DNA.
DR   STRING; 298653.Franean1_0348; -.
DR   EnsemblBacteria; ABW09814; ABW09814; Franean1_0348.
DR   KEGG; fre:Franean1_0348; -.
DR   eggNOG; ENOG4107R1M; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000167538; -.
DR   KO; K01881; -.
DR   OMA; EVYWVTH; -.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LF69.
DR   SWISS-2DPAGE; A8LF69.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571,
KW   ECO:0000313|EMBL:ABW09814.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313}.
FT   DOMAIN       34    283       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   471 AA;  51641 MW;  90E01A3359F05C70 CRC64;
     MDDVAVLTPR STDFPRWYQD VLDKAELADN GPVRGTMVIR PYGYALWERM QADVDTRIKA
     AGAVNAYFPL FIPESYLRRE AEHVEGFSPE LAVVTHGGGK ELAEPVVVRP TSETVIGEYM
     AKWTQSYRDL PLLLNQWANV VRWELRPRLF LRTSEFLWQE GHTAHADAAD AAAYARRIAL
     EVYREFMTSV LALPVFVGAK TRKERFAGAI NTMTCEGMMG DGKALQMATS HELGQNFARA
     FDIDFLGPDG GRHLAWTTSW GSSTRMIGGL IMAHGDDNGL RVPPVLAPTQ VVVLPVRDDD
     AVVTKAREIT DALTALGVRA RLDARPGLSF GRRVTDAELK GIPVRVEVGP RDLAAGNVTL
     ARRDTAEKFP VPLGEAAGRV PVLLDEVQAS LYAQALALRD ERTSDVTSLT EAVEAAATGF
     ARLPWRLVGE DGEARLAEDS LTVRCLQTPD GALPTADTRD EDLVCLVARA Y
//

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